BCEM 393 Lecture Notes - Lecture 2: Bovine Serum Albumin, Mercedes-Benz E-Class, Lysine
Lab Lecture 1
PEPTIDE BOND
- Dehydration forms peptide bonds (amide) to link amino acids together
- The alpha amino and alpha carboxyl groups are destroyed
- Dehydration requires energy (from GTP) in the cell
- The equilibrium lies on the side of hydrolysis, but peptide bonds are kinetically stable
POLYPEPTIDE (>10 RESIDUES)
- Backbond of the polypeptide is: -N-Calpha-C-N-Calpha-C-
- Side chains (green) alternate in stereochemistry
- The chain has directionality, and is written from the amino terminal (N-terminus) to the
carboxyl terminal (C-terminus)
PROTEINS
- A protein is a (usually folded) polypeptide composed of more than or equal to 50 amino acid
residues
- The average weight for an amino acid residue is 115 g/mol, therefore, a protein with 50 amino
acid residues has a molecular weight of approximately 5750 g/mol
- Primary structure is the linear sequence of amino acids (residues) polymer formed by linking
amino acid residues with peptide bonds for a particular protein
- Written from N-terminus to C-terminus
AMINO ACID SEQUENCE OF BOVINE INSULIN SHOWING DISULFIDE BONDS
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Document Summary
Dehydration forms peptide bonds (amide) to link amino acids together. The alpha amino and alpha carboxyl groups are destroyed. Dehydration requires energy (from gtp) in the cell. The equilibrium lies on the side of hydrolysis, but peptide bonds are kinetically stable. The chain has directionality, and is written from the amino terminal (n-terminus) to the carboxyl terminal (c-terminus) A protein is a (usually folded) polypeptide composed of more than or equal to 50 amino acid residues. The average weight for an amino acid residue is 115 g/mol, therefore, a protein with 50 amino acid residues has a molecular weight of approximately 5750 g/mol. Primary structure is the linear sequence of amino acids (residues) polymer formed by linking amino acid residues with peptide bonds for a particular protein. Amino acid sequence of bovine insulin showing disulfide bonds. Cys 7 of the a chain is linked to the cys 7 of the b chain.